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PDBsum entry 2wkl

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2wkl
Jmol
Contents
Protein chain
495 a.a.
Ligands
NAG
NAG-NAG ×2
SO4 ×18
Waters ×326
HEADER    HYDROLASE                               15-JUN-09   2WKL
TITLE     VELAGLUCERASE ALFA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE,
COMPND   5  D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE,
COMPND   6  IMIGLUCERASE;
COMPND   7 EC: 3.2.1.45;
COMPND   8 OTHER_DETAILS: GLYCOSYLATION ON ASN19 CHAIN A, ASN146
COMPND   9  CHAIN A AND ON ASN19 CHAIN B
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM, MEMBRANE,
KEYWDS   2 LYSOSOME, HYDROLASE, ICHTHYOSIS, N-NONYL-DEOXYNOJIRIMYCIN,
KEYWDS   3 N-NONYL-DEOXYNOJIRIMYCIN ALTERNATIVE INITIATION, DISULFIDE
KEYWDS   4 BOND, PHARMACEUTICAL, GAUCHER DISEASE, GLYCOSIDASE,
KEYWDS   5 POLYMORPHISM, GLYCOPROTEIN, ALTERNATIVE SPLICING,
KEYWDS   6 ACID-BETA-GLUCOSIDASE, LIPID METABOLISM, DISEASE MUTATION,
KEYWDS   7 VELAGLUCERASE ALFA
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.BRUMSHTEIN,P.SALINAS,B.PETERSON,V.CHAN,I.SILMAN,
AUTHOR   2 J.L.SUSSMAN,P.J.SAVICKAS,G.S.ROBINSON,A.H.FUTERMAN
REVDAT   2   08-DEC-09 2WKL    1       COMPND JRNL
REVDAT   1   22-SEP-09 2WKL    0
JRNL        AUTH   B.BRUMSHTEIN,P.SALINAS,B.PETERSON,V.CHAN,I.SILMAN,
JRNL        AUTH 2 J.L.SUSSMAN,P.J.SAVICKAS,G.S.ROBINSON,A.H.FUTERMAN
JRNL        TITL   CHARACTERIZATION OF GENE-ACTIVATED HUMAN ACID-
JRNL        TITL 2 BETA-GLUCOSIDASE: CRYSTAL STRUCTURE, GLYCAN
JRNL        TITL 3 COMPOSITION AND INTERNALIZATION INTO MACROPHAGES.
JRNL        REF    GLYCOBIOLOGY                  V.  20    24 2010
JRNL        REFN                   ISSN 0959-6658
JRNL        PMID   19741058
JRNL        DOI    10.1093/GLYCOB/CWP138
REMARK   2
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0067
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.98
REMARK   3   NUMBER OF REFLECTIONS             : 37776
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.17602
REMARK   3   R VALUE            (WORKING SET) : 0.17293
REMARK   3   FREE R VALUE                     : 0.23392
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1995
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.700
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.769
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2682
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK   3   BIN R VALUE           (WORKING SET) : 0.229
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.317
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7781
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 160
REMARK   3   SOLVENT ATOMS            : 326
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 37.7
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.838
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.01
REMARK   3    B22 (A**2) : 0.00
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.629
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.301
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.199
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.819
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8170 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11159 ; 1.494 ; 1.965
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   988 ; 6.468 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   349 ;36.460 ;23.324
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1225 ;17.676 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;25.213 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1218 ; 0.093 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6190 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4956 ; 0.551 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8004 ; 1.060 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3211 ; 1.524 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3155 ; 2.560 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               :   1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    7
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A      26      5
REMARK   3           1     B      1       B      26      5
REMARK   3           2     A     32       A      58      5
REMARK   3           2     B     32       B      58      5
REMARK   3           3     A     65       A     311      5
REMARK   3           3     B     65       B     311      5
REMARK   3           4     A    320       A     340      5
REMARK   3           4     B    320       B     340      5
REMARK   3           5     A    349       A     392      5
REMARK   3           5     B    349       B     392      5
REMARK   3           6     A    377       A     379      5
REMARK   3           6     B    377       B     379      5
REMARK   3           7     A    400       A     497      5
REMARK   3           7     B    400       B     497      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1   A     (A):   1864 ;  0.18 ;  0.50
REMARK   3   LOOSE POSITIONAL   1   A     (A):   1775 ;  0.47 ;  5.00
REMARK   3   MEDIUM THERMAL     1   A  (A**2):   1864 ;  0.75 ;  2.00
REMARK   3   LOOSE THERMAL      1   A  (A**2):   1775 ;  0.91 ; 10.00
REMARK   3   MEDIUM POSITIONAL  1   B     (A):   1864 ;  0.18 ;  0.50
REMARK   3   LOOSE POSITIONAL   1   B     (A):   1775 ;  0.47 ;  5.00
REMARK   3   MEDIUM THERMAL     1   B  (A**2):   1864 ;  0.75 ;  2.00
REMARK   3   LOOSE THERMAL      1   B  (A**2):   1775 ;  0.91 ; 10.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS. DISORDERED REGIONS WERE NOT MODELED
REMARK   4
REMARK   4 2WKL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-09.
REMARK 100 THE PDBE ID CODE IS EBI-40101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39866
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.70
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.5
REMARK 200  R MERGE                    (I) : 0.13
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.6
REMARK 200  R MERGE FOR SHELL          (I) : 0.44
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.66
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2V3F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M (NH4)2SO4/0.1 M HEPES, PH
REMARK 280  7.0, 0.5% (W/V) PEG8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.84650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.84650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       54.68550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.77600
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.68550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.77600
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.84650
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.68550
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.77600
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.84650
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.68550
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.77600
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     PHE A    31
REMARK 465     ALA A   318
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ASN A  59    OD1  ND2
REMARK 470     LYS A 155    CD   CE   NZ
REMARK 470     GLN A 166    CG   CD   OE1  NE2
REMARK 470     LYS A 224    CE   NZ
REMARK 470     GLU A 300    CD   OE1  OE2
REMARK 470     PHE A 347    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLN A 350    OE1  NE2
REMARK 470     LYS A 441    CG   CD   CE   NZ
REMARK 470     LYS A 466    CD   CE   NZ
REMARK 470     ASN B  59    CG   OD1  ND2
REMARK 470     GLU B  72    CD   OE1  OE2
REMARK 470     LYS B 155    CD   CE   NZ
REMARK 470     ARG B 211    CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 224    CE   NZ
REMARK 470     GLN B 226    CD   OE1  NE2
REMARK 470     LYS B 346    CE   NZ
REMARK 470     PHE B 397    CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS B 408    CE   NZ
REMARK 470     LYS B 441    CE   NZ
REMARK 470     LYS B 466    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NH1  ARG A   285  -  O    PRO A   319              1.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  19     -159.61   -145.80
REMARK 500    MET A  49       47.41     38.39
REMARK 500    GLN A  70       70.68   -115.53
REMARK 500    PHE A  75     -145.21   -116.22
REMARK 500    ASN A 117       16.62   -145.79
REMARK 500    ALA A 124     -161.02     76.25
REMARK 500    CYS A 126     -156.75   -127.21
REMARK 500    TYR A 133      147.23   -175.57
REMARK 500    ASN A 146       36.33    -98.66
REMARK 500    LEU A 156      -66.59   -123.16
REMARK 500    ASN A 192     -167.28   -124.81
REMARK 500    GLU A 233      128.48    160.03
REMARK 500    GLU A 235       66.42     33.91
REMARK 500    LEU A 281      -84.77     73.93
REMARK 500    THR A 323      -79.23   -121.67
REMARK 500    CYS A 342      164.88    175.74
REMARK 500    HIS A 374       -6.79     81.28
REMARK 500    TRP A 381     -134.00    -77.99
REMARK 500    ASN A 396       44.36    -88.06
REMARK 500    GLN A 440      147.08    175.13
REMARK 500    TYR A 487       62.22     60.30
REMARK 500    ASN B  19     -150.84   -141.63
REMARK 500    PHE B  75     -141.34   -127.47
REMARK 500    ASN B 117       18.70   -148.27
REMARK 500    ALA B 124     -154.70     77.31
REMARK 500    TYR B 133      151.73    174.22
REMARK 500    ALA B 136       71.08   -154.96
REMARK 500    LEU B 156      -70.36   -109.57
REMARK 500    TRP B 179      -62.21    -91.28
REMARK 500    ASN B 192     -159.82   -127.02
REMARK 500    GLU B 233      133.22    176.80
REMARK 500    TYR B 244      125.59    -39.70
REMARK 500    LEU B 249      109.62   -160.50
REMARK 500    ASN B 270       29.16    -78.69
REMARK 500    LEU B 281      -83.10     70.29
REMARK 500    TYR B 313      -57.05    -19.37
REMARK 500    LEU B 314       40.95   -106.50
REMARK 500    THR B 323      -77.40   -112.81
REMARK 500    SER B 345     -176.60    -58.34
REMARK 500    SER B 351     -108.36     67.73
REMARK 500    HIS B 374        5.93     82.67
REMARK 500    TRP B 381     -139.94    -78.40
REMARK 500    ASP B 405       79.18   -112.95
REMARK 500    ASP B 409       49.31     33.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 CYS B  342     VAL B  343                 -147.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    VAL B 343        23.8      L          L   OUTSIDE RANGE
REMARK 500    SER B 351        21.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC", "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1509
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V3F   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT
REMARK 900 RELATED ID: 1Y7V   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN ACID-BETA-
REMARK 900  GLUCOSIDASE COVALENTLYBOUND TO CONDURITOL B
REMARK 900  EPOXIDE
REMARK 900 RELATED ID: 2J25   RELATED DB: PDB
REMARK 900  PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE
REMARK 900 RELATED ID: 2V3E   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-NONYL-
REMARK 900  DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 2F61   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED
REMARK 900  ACID BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 2V3D   RELATED DB: PDB
REMARK 900  ACID-BETA-GLUCOSIDASE WITH N-BUTYL-
REMARK 900  DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 1OGS   RELATED DB: PDB
REMARK 900  HUMAN ACID-BETA-GLUCOSIDASE
DBREF  2WKL A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2WKL B    1   497  UNP    P04062   GLCM_HUMAN      40    536
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 A  497  ARG ARG GLN
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 B  497  ARG ARG GLN
HET    NAG  A1498      14
HET    NAG  A1499      14
HET    NAG  A1500      14
HET    NAG  B1498      14
HET    NAG  B1499      14
HET    SO4  B1500       5
HET    SO4  B1501       5
HET    SO4  A1501       5
HET    SO4  A1502       5
HET    SO4  B1502       5
HET    SO4  A1503       5
HET    SO4  A1504       5
HET    SO4  A1505       5
HET    SO4  B1503       5
HET    SO4  A1506       5
HET    SO4  B1504       5
HET    SO4  B1505       5
HET    SO4  B1506       5
HET    SO4  B1507       5
HET    SO4  A1507       5
HET    SO4  B1508       5
HET    SO4  A1508       5
HET    SO4  A1509       5
HETNAM     SO4 SULFATE ION
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   3  SO4    18(O4 S 2-)
FORMUL   4  NAG    5(C8 H15 N O6)
FORMUL   5  HOH   *326(H2 O1)
HELIX    1   1 THR A   86  ALA A   95  1                                  10
HELIX    2   2 SER A   97  SER A  110  1                                  14
HELIX    3   3 PRO A  150  LYS A  155  1                                   6
HELIX    4   4 LEU A  156  ALA A  168  1                                  13
HELIX    5   5 PRO A  182  LEU A  185  5                                   4
HELIX    6   6 ASP A  203  HIS A  223  1                                  21
HELIX    7   7 GLU A  235  LEU A  241  5                                   7
HELIX    8   8 THR A  252  ASP A  263  1                                  12
HELIX    9   9 ASP A  263  ASN A  270  1                                   8
HELIX   10  10 LEU A  286  LEU A  288  5                                   3
HELIX   11  11 PRO A  289  THR A  297  1                                   9
HELIX   12  12 ASP A  298  LYS A  303  1                                   6
HELIX   13  13 THR A  323  PHE A  331  1                                   9
HELIX   14  14 SER A  356  TYR A  373  1                                  18
HELIX   15  15 ILE A  406  ASP A  409  5                                   4
HELIX   16  16 GLN A  414  LYS A  425  1                                  12
HELIX   17  17 THR B   86  ALA B   95  1                                  10
HELIX   18  18 SER B   97  SER B  110  1                                  14
HELIX   19  19 PRO B  150  LYS B  155  1                                   6
HELIX   20  20 LEU B  156  ALA B  168  1                                  13
HELIX   21  21 PRO B  182  LEU B  185  5                                   4
HELIX   22  22 ASP B  203  HIS B  223  1                                  21
HELIX   23  23 SER B  237  LEU B  241  5                                   5
HELIX   24  24 THR B  252  ASP B  263  1                                  12
HELIX   25  25 ASP B  263  ASN B  270  1                                   8
HELIX   26  26 LEU B  286  LEU B  288  5                                   3
HELIX   27  27 PRO B  289  THR B  297  1                                   9
HELIX   28  28 ASP B  298  LYS B  303  1                                   6
HELIX   29  29 THR B  323  PHE B  331  1                                   9
HELIX   30  30 SER B  356  LEU B  372  1                                  17
HELIX   31  31 ILE B  406  ASP B  409  5                                   4
HELIX   32  32 GLN B  414  LYS B  425  1                                  12
SHEET    1  AA 4 PRO A   6  LYS A   7  0
SHEET    2  AA 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412
SHEET    1  AB 9 GLU A  50  PRO A  55  0
SHEET    2  AB 9 THR A  36  THR A  43 -1  O  PHE A  37   N  GLY A  54
SHEET    3  AB 9 SER A 488  TRP A 494 -1  O  ILE A 489   N  SER A  42
SHEET    4  AB 9 ALA A 456  ASN A 462 -1  O  ALA A 456   N  TRP A 494
SHEET    5  AB 9 LEU A 444  MET A 450 -1  O  ASP A 445   N  LEU A 461
SHEET    6  AB 9 GLN A 432  ALA A 438 -1  O  GLN A 432   N  MET A 450
SHEET    7  AB 9 LEU A  66  LYS A  77 -1  O  THR A  68   N  VAL A 437
SHEET    8  AB 9 VAL A 468  ASP A 474  1  O  THR A 471   N  LEU A  67
SHEET    9  AB 9 GLY A 478  SER A 484 -1  O  GLY A 478   N  ASP A 474
SHEET    1  AC 9 GLY A  80  ALA A  84  0
SHEET    2  AC 9 GLY A 377  ASN A 382  1  O  TRP A 378   N  GLY A  82
SHEET    3  AC 9 MET A 335  CYS A 342  1  O  ALA A 338   N  THR A 379
SHEET    4  AC 9 GLY A 307  TYR A 313  1  O  ILE A 308   N  PHE A 337
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120
SHEET    1  BA 4 PRO B   6  LYS B   7  0
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412
SHEET    1  BB 9 GLU B  50  PRO B  55  0
SHEET    2  BB 9 THR B  36  THR B  43 -1  O  PHE B  37   N  GLY B  54
SHEET    3  BB 9 SER B 488  TRP B 494 -1  O  ILE B 489   N  SER B  42
SHEET    4  BB 9 ALA B 456  ASN B 462 -1  O  ALA B 456   N  TRP B 494
SHEET    5  BB 9 LEU B 444  MET B 450 -1  O  ASP B 445   N  LEU B 461
SHEET    6  BB 9 GLN B 432  ALA B 438 -1  O  GLN B 432   N  MET B 450
SHEET    7  BB 9 LEU B  65  LYS B  77 -1  O  THR B  68   N  VAL B 437
SHEET    8  BB 9 VAL B 468  ASP B 474  1  O  PRO B 469   N  LEU B  65
SHEET    9  BB 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474
SHEET    1  BC 9 GLY B  80  ALA B  84  0
SHEET    2  BC 9 VAL B 375  ASN B 382  1  O  TRP B 378   N  GLY B  82
SHEET    3  BC 9 MET B 335  GLU B 340  1  O  LEU B 336   N  VAL B 376
SHEET    4  BC 9 GLY B 307  HIS B 311  1  O  ILE B 308   N  PHE B 337
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  ALA B 176   N  THR B 231
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.08
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.09
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.06
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.07
LINK         ND2 ASN A  19                 C1  NAG A1499     1555   1555  1.44
LINK         ND2 ASN A 146                 C1  NAG A1498     1555   1555  1.45
LINK         O4  NAG A1499                 C1  NAG A1500     1555   1555  1.45
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.44
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.42
CISPEP   1 LEU A  288    PRO A  289          0         5.60
CISPEP   2 GLY A  390    PRO A  391          0         9.37
CISPEP   3 LEU B  288    PRO B  289          0         4.04
CISPEP   4 GLY B  390    PRO B  391          0         2.62
SITE     1 AC1  5 HIS A 145  ASN A 146  HOH A2142  SER B  97
SITE     2 AC1  5 PRO B  98
SITE     1 AC2  3 ASN A  19  NAG A1500  HOH A2143
SITE     1 AC3  1 NAG A1499
SITE     1 AC4  5 ASN B  19  TYR B  22  NAG B1499  HOH B2173
SITE     2 AC4  5 HOH B2174
SITE     1 AC5  2 NAG B1498  HOH B2175
SITE     1 AC6  6 TYR B  11  SER B  12  ARG B 353  SER B 356
SITE     2 AC6  6 TRP B 357  ASP B 358
SITE     1 AC7  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     2 AC7  6 HOH B2176  HOH B2177
SITE     1 AC8  4 LYS A  79  TRP A 228  ARG A 277  HIS A 306
SITE     1 AC9  6 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC9  6 TRP A 357  ASP A 358
SITE     1 BC1  4 ARG B 170  PRO B 428  HIS B 451  HOH B2178
SITE     1 BC2  4 LYS A 321  ARG A 329  ARG B 329  LEU B 330
SITE     1 BC3  4 GLY A 193  LYS A 194  SER A 242  GLY A 243
SITE     1 BC4  3 ARG A  44  SER A  45  HOH A2144
SITE     1 BC5  3 ARG B  44  SER B  45  HOH B2179
SITE     1 BC6  3 ARG A  44  SER A 465  TYR A 487
SITE     1 BC7  5 THR B  63  GLY B  64  GLN B 440  LYS B 473
SITE     2 BC7  5 HOH B2180
SITE     1 BC8  3 ARG B  44  SER B 465  TYR B 487
SITE     1 BC9  2 GLU B 254  ARG B 257
SITE     1 CC1  3 HIS B 290  LYS B 293  HOH B2181
SITE     1 CC2  1 ARG A 277
SITE     1 CC3  4 ARG A 262  ALA B   1  ARG B   2  HOH B2001
SITE     1 CC4  3 ARG A 170  PRO A 428  HIS A 451
SITE     1 CC5  3 SER A  45  ARG A  47  HOH A2145
CRYST1  109.371  285.552   91.693  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.009143  0.000000  0.000000        0.00000
SCALE2      0.000000  0.003502  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010906        0.00000
      
PROCHECK
Go to PROCHECK summary
 References